The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (315 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Export to BibTeX Export to EndNote
Paper type: Erratum, Journal Article,
Impact factor: 8.209, 5-year impact factor: 7.139
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-36148946799&partnerID=40&md5=10c74ed9da215a38e7c0d1ef7e944167
Keywords: Glutaredoxin, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Thioredoxin, Catalysis, Chimera, Disulfide Bond, Homeostasis, Human, Mesophilic Bacterium, Nonhuman, Nucleotide Sequence, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Analysis, Protein Folding, Protein Function, Protein Structure, Review, Thermophile, Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Disulfide-Isomerase, Sequence Homology, Bacteria (microorganisms), Eukaryota, Prokaryota, Erratum,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Complesso Universitario Monte S. Angelo, Naples, Italy
Dip. Biologia Strutturale e Funzionale, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Naples, Italy
References:
Amegbey, G.Y., Monzavi, H., Habibi-Nazhad, B., Bhattacharyya, S., Wishart, D.S., Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum (2003) Biochemistry, 42, pp. 8001-801
Anken, E., Braakman, I., Versatility of the endoplasmic reticulum protein folding factory (2005) Crit Rev Biochem Mol Biol, 40, pp. 191-228
Arcari, P., Fasullo, L., Masullo, M., Catanzano, F., Bocchini, V.A., NAD(P)H oxidase isolated from the archaeon Sulfolobus solfataricus is not homologous with another NADH oxidase present in the same microorganism biochemical characterization of the enzyme and cloning of the encoding gene (2000) J Biol Chem, 275, pp. 895-900
Arscott, L.D., Gromer, S., Schirmer, R.H., Becker, K., Williams Jr., C.H., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli (1997) Proc Natl Acad Sci U S A, 94, pp. 3621-3626
Bartolucci, S., Guagliardi, A., Pedone, E., De Pascale, D., Cannio, R., Camardella, L., Rossi, M., Nicolini, C., Thioredoxin from Bacillus acidocaldarius: Characterization, high-level expression in Escherichia coli and molecular modelling (1997) Biochem J, 328, pp. 277-285
Bartolucci, S., De Pascale, D., Rossi, M., Protein disulfide oxidoreductase from Pyrococcus furiosus: Biochemical properties (2001) Methods Enzymol, 334, pp. 62-73
Beeby, M., O'Connor, B.D., Ryttersgaard, C., Boutz, D.R., Perry, L.J., Yeates, T.O., The genomics of disulfide bonding and protein stabilization in thermophiles (2005) PLoS Biol, 3, pp. 1549-1558
Bhattacharyya, S., Habibi-Nazhad, B., Amegbey, G., Slupsky, C.M., Yee, A., Arrowsmith, C., Wishart, D.S., Identification of a novel archaebacterial thioredoxin: Determination of function through structure (2002) Biochemistry, 41, pp. 4760-4770
Bjornstedt, M., Hamberg, M., Kumar, S., Xue, J., Holmgren, A., Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols (1995) J Biol Chem, 270, pp. 11761-11764
Bjornstedt, M., Kumar, S., Bjorkhem, L., Spyrou, G., Holmgren, A., Selenium and the thioredoxin and glutaredoxin systems (1997) Biomed Environ Sci, 10, pp. 271-279
Buettner, C., Harney, J.W., Berry, M.J., The Caenorhabditis elegans homologue of thioredoxin reductase contains a selenocysteine insertion sequence (SECIS) element that differs from mammalian SECIS elements but directs selenocysteine incorporation (1999) J Biol Chem, 274, pp. 21598-21602
Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M.R., Bulleid, N.J., Sitia, R., ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum (2000) J Biol Chem, 275, pp. 4827-4833
Cannio, R., Fiorentino, G., Carpinelli, P., Rossi, M., Bartolucci, S., Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species (1996) J Bacteriol, 178, pp. 301-305
Chae, H.Z., Chung, S.J., Rhee, S.G., Thioredoxin dependent peroxide reductase from yeast (1994) J Biol Chem, 269, pp. 27670-27678
D'Ambrosio, K., De Simone, G., Pedone, E., Rossi, M., Bartolucci, S., Pedone, C., Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus (2004) Acta Cryst, D60, pp. 2076-2077
D'Ambrosio, K., Pedone, E., Langella, E., De Simone, G., Rossi, M., Pedone, C., Bartolucci, S., A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (2006) J Mol Biol, 362, pp. 743-752
Darby, N.J., Kemmink, J., Creighton, T.E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Dijkstra, K., Karvonen, P., Pirneskoski, A., Koivunen, P., Kivirikko, K.I., Darby, N.J., van Straaten, M., Kemmink, J., Assignment of 1H, 13C and 15N resonances of the a′ domain of protein disulfide isomerase (1999) J Biomol NMR, 14, pp. 195-196
Dixon, D.P., Van Lith, M., Edwards, R., Benham, A., Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins (2003) Antioxid Redox Signal, 5, pp. 389-396
Fabianek, R.A., Hennecke, H., Thony-Meyer, L., Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli (2000) FEMS Microbiol Rev, 24, pp. 303-316
Ferrari, D.M., Söling, H.D., The protein disulphide-isomerase family: Unraveling a string of folds (1999) Biochem J, 339, pp. 1-10
Freedman, R.B., Novel disulfide oxidoreductase in search of a function (1998) Nat Struct Biol, 5, pp. 531-532
Freedman, R.B., Klappa, P., Ruddock, L.W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Rep, 3, pp. 136-140
Fuchs, J.A., (1989) Glutathione: Chemical, biochemical, and medical aspects, p. 551. , Edited by Dolphin D, Poulsen R, and Avramovic O. New York: John Wiley and Sons, Part B, p
Ghaemmaghami, S., Huh, W.K., Bower, K., Howson, R.W., Belle, A., Dephoure, N., O'Shea, E.K., Weissman, J.S., Global analysis of protein expression in yeast (2003) Nature, 425, pp. 737-741
Ghisla, S., Massey, V., Mechanisms of flavoprotein catalyzed reactions (1989) Eur J Biochem, 181, pp. 1-17
Gladyshev, V.N., Jeang, K.T., Stadtman, T.C., Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene (1996) Proc Natl Acad Sci U S A, 93, pp. 6146-6151
Gleason, F.K., Holmgren, A., Thioredoxin and related proteins in procaryotes (1988) FEMS Microbiol Rev, 4, pp. 271-297
Grauschopf, U., Winther, J.R., Korber, P., Zander, T., Dallinger, P., Bardwell, J.C., Why is DsbA such an oxidizing disulfide catalyst? (1995) Cell, 83, pp. 947-955
Grauschopf, U., Fritz, A., Glockshuber, R., Mechanism of the electron transfer catalyst DsbB from Escherichia coli (2003) EMBO J, 22, pp. 3503-3513
Gromer, S., Merkle, H., Schirmer, R.H., Becker, K., Human placenta thioredoxin reductase: Preparation and inhibitor studies (2002) Methods Enzymol, 347, pp. 382-394
Gross, E., Sevier, C.S., Vala, A., Kaiser, C.A., Fass, D., A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p (2002) Nat Struct Biol, 9, pp. 61-67
Gross, E., Kastner, D.B., Kaiser, C.A., Fass, D., Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell (2004) Cell, 117, pp. 601-610
Guagliardi, A., De Pascale, D., Cannio, R., Nobile, V., Bartolucci, S., Rossi, M., The purification, cloning, and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (1995) J Biol Chem, 270, pp. 5748-5755
Guthapfel, R., Gueguen, P., Quemeneur, E., ATP binding and hydrolysis by the multifunctional protein disulfide isomerase (1996) J Biol Chem, 271, pp. 2663-2666
Holmgren, A., Bjornstedt, M., Thioredoxin and thioredoxin reductase (1995) Methods Enzymol, 252, pp. 199-208
Holmgren, A., Johansson, C., Berndt, C., Lonn, M.E., Hudemann, C., Lillig, C.H., Thiol redox control via thioredoxin and glutaredoxin systems (2005) Biochem Soc Trans, 33, pp. 1375-1377
Jeon, S.J., Ishikawa, K., Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1 (2002) Eur J Biochem, 269, pp. 5423-5430
Kadokura, H., Katzen, F., Beckwith, J., Protein disulfide bond formation in prokaryotes (2003) Annu Rev Biochem, 72, pp. 111-135
Kashima, Y., Ishikawa, K., Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from Pyrococcus horikoshii (2003) J Biochem (Tokyo), 134, pp. 25-29
Kawakami, R., Sakuraba, H., Kamohara, S., Goda, S., Kawarabayasi, Y., Ohshima, T., Oxidative stress response in an anaerobic hyperthermophilic archaeon: Presence of a functional peroxiredoxin in Pyrococcus horikoshii (2004) J Biochem (Tokyo), 136, pp. 541-547
Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., Creighton, T.E., Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy (1996) Biochemistry, 35, pp. 7684-7691
Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R.M., Penka, E., Nilges, M., Darby, N.J., The structure in solution of the b domain of protein disulfide isomerase (1999) J Biomol NMR, 13, pp. 357-368
Kortemme, T., Darby, N.J., Creighton, T.E., Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 14503-14511
Lappi, A., Lensink, M., Alanen, H., Salo, K., Lobell, M., Juffer, A., Ruddock, L., A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases (2004) J Mol Biol, 335, pp. 283-295
Lee, D.Y., Ahn, B.Y., Kim, K.S., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Lemaire, S.D., Miginiac-Maslow, M., The thioredoxin superfamily in Chlamydomonas reinhardtii (2004) Photosynth Res, 82, pp. 203-220
Li, K., Pasternak, C., Klug, G., Expression of the trxA gene for thioredoxin 1 in Rhodobacter sphaeroides during oxidative stress (2003) Arch Microbiol, 180, pp. 484-489
Limauro, D., Pedone, E., Pirone, L., Bartolucci, S., Identification and characterization of 1-Cys peroxiredoxin from Sulfolobus solfataricus and its involvement in the response to oxidative stress (2006) FEBS J, 273, pp. 721-731
Mallick, P., Boutz, D.R., Eisenberg, D., Yeates, T.O., Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds (2002) Proc Natl Acad Sci U S A, 99, pp. 9679-9684
Martin, J.L., Bardwell, J.C., Kuriyan, J., Crystal structure of the DsbA protein required for disulphide bond formation in vivo (1993) Nature, 365, pp. 464-468
Martin, J.L., Thioredoxin: A fold for all reasons (1995) Structure, 3, pp. 245-250
McFarlan, S.C., Terrell, C.A., Hogenkamp, H.P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J Biol Chem, 267, pp. 10561-10569
Meister, A., Glutathione metabolism and its selective modification (1988) J Biol Chem, 263, pp. 17205-17208
Messens, J., Collet, J.F., Pathways of disulfide bond formation in Escherichia coli (2006) Int J Biochem Cell Biol, 38, pp. 1050-1062
Miranda-Vizuete, A., Damdimopoulos, A.E., Gustafsson, J., Spyrou, G., Cloning, expression, and characterization of a novel Escherichia coli thioredoxin (1997) J Biol Chem, 272, pp. 30841-30847
Mittard, V., Blackledge, M.J., Stein, M., Jacquot, J.P., Marion, D., Lancelin, J.M., NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii (1997) Eur J Biochem, 243, pp. 374-383
Mizohata, E., Sakai, H., Fusatomi, E., Terada, T., Murayama, K., Shirouzu, M., Yokoyama, S., Crystal structure of an archaeal peroxiredoxin from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix K1 (2005) J Mol Biol, 354, pp. 317-329
Moore EC, Reichard P, and Thelander L. Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B. J Biol Chem 239: 3445-3452, 1964Moutevelis, E., Warwickwe, J., Prediction of pKa and redox properties in the thioredoxin superfamily (2004) Protein Sci, 13, pp. 2744-2752
Nicastro, G., de Chiara, C., Pedone, E., Tato', M., Rossi, M., Bartolucci, S., NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius: Possible determinants of protein stability (2000) Eur J Biochem, 267, pp. 403-413
Pedone, E., Bartolucci, S., Rossi, M., Saviano, M., Computational analysis of the thermal stability in thioredoxins: A molecular dynamics approach (1998) J Biomol Struct Dynamics, 16, pp. 437-446
Pedone, E., Cannio, R., Saviano, M., Rossi, M., Bartolucci, S., Prediction and experimental testing of Bacillus acidocaldarius thioredoxin stability (1999) Biochem J, 339, pp. 309-317
Pedone, E., Ren, B., Ladenstein, R., Rossi, M., Bartolucci, S., Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus (2004) Eur J Biochem, 271, pp. 3437-3448
Pedone, E., D'Ambrosio, K., De Simone, G., Rossi, M., Pedone, C., Bartolucci, S., Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (2006) J Mol Biol, 356, pp. 155-164
Pedone, E., Limauro, D., D'Alterio, R., Rossi, M., Bartolucci, S., Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (2006) FEBS J, 273, pp. 5407-5420
Prieto-Alamo, M.J., Jurado, J., Gallardo-Madueno, R., Monje-Casas, F., Holmgren, A., Pueyo, C., Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress (2000) J Biol Chem, 275, pp. 13398-13405
Prinz, W.A., Aslund, F., Holmgren, A., Beckwith, J., The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm (1997) J Biol Chem, 272, pp. 15661-15667
Prongay, A.J., Engelke, D.R., Williams Jr., C.H., Characterization of two active site mutations of thioredoxin reductase from Escherichia coli (1989) J Biol Chem, 264, pp. 2656-2664
Quemeneur, E., Guthapfel, R., Gueguen, P., A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase (1994) J Biol Chem, 269, pp. 5485-5488
Raczko, A.M., Bujnicki, J.M., Pawlowski, M., Godlewska, R., Lewandowska, M., Jagusztyn-Krynicka, E.K., Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria (2005) Microbiology, 151, pp. 219-223
Rehse, P.H., Kumei, M., Tahirov, T.H., Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus (2005) Proteins, 61, pp. 1032-1037
Ren, B., Tibbelin, G., De Pascale, D., Rossi, M., Bartolucci, S., Ladenstein, R., Crystallization and preliminary X-ray structure analysis of a hyperthermostable thioltransferase from the archaeon Pyrococcus furiosus (1997) J Struct Biol, 119, pp. 1-5
Reynolds, C.M., Meyer, J., Poole, L.B., An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum (2002) Biochemistry, 41, pp. 1990-2001
Rietsch, A., Belin, D., Martin, N., Beckwith, J., An in vivo pathway for disulfide bond isomerization in Escherichia coli (1996) Proc Natl Acad Sci U S A, 93, pp. 13048-13053
Rigobello, M.P., Scutari, G., Folda, A., Bindoli, A., Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c (2004) Biochem Pharmacol, 67, pp. 689-696
Rossmann, R., Stern, D., Loferer, H., Jacobi, A., Glockshuber, R., Hennecke, H., Replacement of Pro109 by His in TlpA, a thioredoxin-like protein from Bradyrhizobium japonicum, alters its redox properties but not its in vivo functions (1997) FEBS Lett, 406, pp. 249-254
Rouhier, N., Gelhaye, E., Sautiere, P.E., Brun, A., Laurent, P., Tagu, D., Gerard, J., Jacquot, J.P., Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor (2001) Plant Physiol, 127, pp. 1299-1309
Ruddock, L.W., Hirst, T.R., Feedman, R.B., pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1995) Biochem J, 315, pp. 1000-1005
Ruocco, M.R., Ruggiero, A., Masullo, L., Arcari, P., Masullo, M.A., 35 kDa NAD(P)H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase (2004) Biochimie, 86, pp. 883-892
Saarinen, M., Gleason, F.K., Eklund, H., Crystal structure of thioredoxin-2 from Anabaena (1995) Structure, 3, pp. 1097-1108
Sevier, C.S., Cuozzo, J.W., Vala, A., Aslund, F., Kaiser, C.A., A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation (2001) Nat Cell Biol, 3, pp. 874-882
Sevier, C.S., Kaiser, C.A., Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 (2006) Mol Biol Cell, 17, pp. 2256-2266
She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez M J, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A., Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, and Van der Oost J. The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc Natl Acad Sci U S A 8: 7835-7840, 2001Silva, G., LeGall, J., Xavier, A.V., Teixeira, M., Rodrigues-Pousada, C., Molecular characterization of Desulfovibrio gigas neelaredoxin, a protein involved in oxygen detoxification in anaerobes (2001) J Bacteriol, 183, pp. 4413-4420
Sitia, R., Braakman, I., Quality control in the endoplasmic reticulum protein factory (2003) Nature, 426, pp. 891-894
Song, J., Quan, H., Wang, C., Dependence of anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochem J, 328, pp. 841-846
Tamura, T., Stadtman, T.C., A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity (1996) Proc Natl Acad Sci U S A, 3, pp. 1006-1011
Tian, G., Xiang, S., Noiva, R., Lennarz, W.J., Schindelin, H., The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites (2006) Cell, 124, pp. 61-73
Vala, A., Sevier, C.S., Kaiser, C.A., Structural determinants of substrate access to the disulfide oxidase Erv2p (2005) J Mol Biol, 354, pp. 952-966
Wang, P.F., Arscott, L.D., Gilberger, T.W., Muller, S., Williams Jr., C.H., Thioredoxin reductase from Plasmodium falciparum: Evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol (1999) Biochemistry, 38, pp. 3187-3196
Wilkinson, B., Gilbert, H.F., Protein disulfide isomerase (2004) Biochim Biophys Acta, 1699, pp. 35-44
Wood, Z.A., Schroder, E., Robin Harris, J., Poole, L.B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Wunderlich, M., Glockshuber, R., Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli (1993) Protein Sci, 2, pp. 717-726
Zillig, W., Palm, P., Reiter, W.D., Gropp, F., Puhler, G., Klenk, H.P., Comparative evaluation of gene expression in archaebacteria (1988) Eur J Biochem, 173, pp. 473-482
Carvalho, A.P., Fernandes, P.A., Ramos, M.J., Similarities and differences in the thioredoxin superfamily (2006) Prog Bio-phys Mol Biol, 91, pp. 229-248
D'Ambrosio, K., Limauro, D., Pedone, E., Galdi, I., Pedone, C., Bartolucci, S., De Simone, G., Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus (2009) Proteins, 76, pp. 995-1006
Digilio, F.A., Morra, R., Pedone, E., Bartolucci, S., Rossi, M., High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (2003) Protein Expr Purif, 30, pp. 179-184
Gruber, C.W., Cemazar, M., Heras, B., Martin, J.L., Craik, D.J., Protein disulfide isomerase: The structure of oxidative folding (2006) Trends Biochem Sci, 31, pp. 455-464
Guagliardi, A., Cerchia, L., De Rosa, M., Rossi, M., Barto-Lucci, S., Isolation of a thermostable enzyme catalyzing dis-ulfide bond formation from the archaebacterium Sulfolobus solfataricus (1992) FEBS Lett, 303, pp. 27-30
Guagliardi, A., Nobile, V., Bartolucci, S., Rossi, M., Isolation of a thioredoxin from the extreme thermophilic archae-bacterium Sulfolobus solfataricus (1994) Int J Biochem, 26, pp. 375-380
Jeon, S.-J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) Journal of Biological Chemistry, 278 (26), pp. 24174-24180. , DOI 10.1074/jbc.M300618200
Ladenstein, R., Ren, B., Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles (2006) FEBS J, 273, pp. 4170-4185
Leone, M., Di Lello, P., Ohlenschlager, O., Pedone, E.M., Bartolucci, S., Rossi, M., Di Blasio, B., Fattorusso, R., Solution structure and back-bone dynamics of the K18G=R82E Alicyclobacillus acid-ocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (2004) Biochemistry, 43, pp. 6043-6058
Limauro, D., Fiorentino, G., Bartolucci, S., How Sulfolobus responds to enviromental stress Biochemistry and Molecular Biology in the Thermophilic Archaeon S. Solfataricus, , Edited by Farina B and Faraone Mennella MR. Chapter 6: 105-130 2004. Research Signpost T.C. 37=661 (2) Fort P.O., Trivandrum-695 023, Kerala, India
Limauro, D., Saviano, M., Galdi, I., Rossi, M., Bartolucci, S., Pedone, E., Sulfolobus solfataricus protein disulphide oxido-reductase: Insight into the roles of its redox sites (2009) Protein Eng des Sel, 22, pp. 19-26
Moore, E.C., Reichard, P., Thelander, L., Enzymatic synthesis of deoxyribonucleotides.V. Purification and properties of thioredoxin reductase from Escherichia coli B (1964) J Biol Chem, 239, pp. 3445-3452
Raia, C.A., Guagliardi, A., D'Auria, S., Bartolucci, S., De Rosa, M., Rossi, M., Characterization of redox proteins from extreme thermophilic archaebacteria: Studies on alcohol dehydrogenase and thioredoxins (1995) Biosensors Bioelectron, 10, pp. 135-140
Ritz, D., Pate, H., Doan, B., Zheng, M., Aslund, F., Storz, G., Beckwith, J., Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli (2000) J Biol Chem, 275, pp. 2505-2512
She, Q., Singh, R.K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M.J., Chan-Weiher, C.C.-Y., Van Der Oostg, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (14), pp. 7835-7840. , DOI 10.1073/pnas.141222098
Song, J.-L., Quan, H., Wang, C.-C., Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochemical Journal, 328 (3), pp. 841-846
Amegbey, G. Y., Monzavi, H., Habibi-Nazhad, B., Bhattacharyya, S., Wishart, D. S., Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum (2003) Biochemistry, 42, pp. 8001-801
Arscott, L. D., Gromer, S., Schirmer, R. H., Becker, K., Williams Jr., C. H., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli (1997) Proc Natl Acad Sci U S A, 94, pp. 3621-3626
Chae, H. Z., Chung, S. J., Rhee, S. G., Thioredoxin dependent peroxide reductase from yeast (1994) J Biol Chem, 269, pp. 27670-27678
Darby, N. J., Kemmink, J., Creighton, T. E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Dixon, D. P., Van Lith, M., Edwards, R., Benham, A., Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins (2003) Antioxid Redox Signal, 5, pp. 389-396
Fabianek, R. A., Hennecke, H., Thony-Meyer, L., Periplasmic protein thiol: disulfide oxidoreductases of Escherichia coli (2000) FEMS Microbiol Rev, 24, pp. 303-316
Ferrari, D. M., S ling, H. D., The protein disulphide-isomerase family: Unraveling a string of folds (1999) Biochem J, 339, pp. 1-10
Freedman, R. B., Novel disulfide oxidoreductase in search of a function (1998) Nat Struct Biol, 5, pp. 531-532
Freedman, R. B., Klappa, P., Ruddock, L. W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Rep, 3, pp. 136-140
Fuchs, J. A., (1989) Glutathione: Chemical, biochemical, and medical aspects, p. 551. , Edited by Dolphin D, Poulsen R, and Avramovic O. New York: John Wiley and Sons, Part B, p
Gladyshev, V. N., Jeang, K. T., Stadtman, T. C., Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene (1996) Proc Natl Acad Sci U S A, 93, pp. 6146-6151
Gleason, F. K., Holmgren, A., Thioredoxin and related proteins in procaryotes (1988) FEMS Microbiol Rev, 4, pp. 271-297
Jeon, S. J., Ishikawa, K., Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1 (2002) Eur J Biochem, 269, pp. 5423-5430
Lee, D. Y., Ahn, B. Y., Kim, K. S., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Lemaire, S. D., Miginiac-Maslow, M., The thioredoxin superfamily in Chlamydomonas reinhardtii (2004) Photosynth Res, 82, pp. 203-220
Martin, J. L., Bardwell, J. C., Kuriyan, J., Crystal structure of the DsbA protein required for disulphide bond formation in vivo (1993) Nature, 365, pp. 464-468
Martin, J. L., Thioredoxin: A fold for all reasons (1995) Structure, 3, pp. 245-250
McFarlan, S. C., Terrell, C. A., Hogenkamp, H. P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J Biol Chem, 267, pp. 10561-10569
Prieto-Alamo, M. J., Jurado, J., Gallardo-Madueno, R., Monje-Casas, F., Holmgren, A., Pueyo, C., Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress (2000) J Biol Chem, 275, pp. 13398-13405
Prinz, W. A., Aslund, F., Holmgren, A., Beckwith, J., The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm (1997) J Biol Chem, 272, pp. 15661-15667
Prongay, A. J., Engelke, D. R., Williams Jr., C. H., Characterization of two active site mutations of thioredoxin reductase from Escherichia coli (1989) J Biol Chem, 264, pp. 2656-2664
Raczko, A. M., Bujnicki, J. M., Pawlowski, M., Godlewska, R., Lewandowska, M., Jagusztyn-Krynicka, E. K., Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria (2005) Microbiology, 151, pp. 219-223
Rehse, P. H., Kumei, M., Tahirov, T. H., Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus (2005) Proteins, 61, pp. 1032-1037
Reynolds, C. M., Meyer, J., Poole, L. B., An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum (2002) Biochemistry, 41, pp. 1990-2001
Rigobello, M. P., Scutari, G., Folda, A., Bindoli, A., Mitochondrial thioredoxin reductase inhibition by gold (I) compounds and concurrent stimulation of permeability transition and release of cytochrome c (2004) Biochem Pharmacol, 67, pp. 689-696
Ruddock, L. W., Hirst, T. R., Feedman, R. B., pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol: disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1995) Biochem J, 315, pp. 1000-1005
Ruocco, M. R., Ruggiero, A., Masullo, L., Arcari, P., Masullo, M. A., 35 kDa NAD (P) H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase (2004) Biochimie, 86, pp. 883-892
Sevier, C. S., Cuozzo, J. W., Vala, A., Aslund, F., Kaiser, C. A., A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation (2001) Nat Cell Biol, 3, pp. 874-882
Sevier, C. S., Kaiser, C. A., Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 (2006) Mol Biol Cell, 17, pp. 2256-2266
Wang, P. F., Arscott, L. D., Gilberger, T. W., Muller, S., Williams Jr., C. H., Thioredoxin reductase from Plasmodium falciparum: Evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol (1999) Biochemistry, 38, pp. 3187-3196
Wood, Z. A., Schroder, E., Robin Harris, J., Poole, L. B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Carvalho, A. P., Fernandes, P. A., Ramos, M. J., Similarities and differences in the thioredoxin superfamily (2006) Prog Bio-phys Mol Biol, 91, pp. 229-248
Digilio, F. A., Morra, R., Pedone, E., Bartolucci, S., Rossi, M., High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (2003) Protein Expr Purif, 30, pp. 179-184
Gruber, C. W., Cemazar, M., Heras, B., Martin, J. L., Craik, D. J., Protein disulfide isomerase: The structure of oxidative folding (2006) Trends Biochem Sci, 31, pp. 455-464
Jeon, S. -J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) Journal of Biological Chemistry, 278 (26), pp. 24174-24180. , DOI 10. 1074/jbc. M300618200
Moore, E. C., Reichard, P., Thelander, L., Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B (1964) J Biol Chem, 239, pp. 3445-3452
Raia, C. A., Guagliardi, A., D'Auria, S., Bartolucci, S., De Rosa, M., Rossi, M., Characterization of redox proteins from extreme thermophilic archaebacteria: Studies on alcohol dehydrogenase and thioredoxins (1995) Biosensors Bioelectron, 10, pp. 135-140
She, Q., Singh, R. K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M. J., Chan-Weiher, C. C. -Y., Van Der Oostg, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (14), pp. 7835-7840. , DOI 10. 1073/pnas. 141222098
Song, J. -L., Quan, H., Wang, C. -C., Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochemical Journal, 328 (3), pp. 841-846
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Export to BibTeX Export to EndNote
Paper type: Erratum, Journal Article,
Impact factor: 8.209, 5-year impact factor: 7.139
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-36148946799&partnerID=40&md5=10c74ed9da215a38e7c0d1ef7e944167
Keywords: Glutaredoxin, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Thioredoxin, Catalysis, Chimera, Disulfide Bond, Homeostasis, Human, Mesophilic Bacterium, Nonhuman, Nucleotide Sequence, Oxidation, Oxidation Reduction Reaction, Priority Journal, Protein Analysis, Protein Folding, Protein Function, Protein Structure, Review, Thermophile, Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Disulfide-Isomerase, Sequence Homology, Bacteria (microorganisms), Eukaryota, Prokaryota, Erratum,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Complesso Universitario Monte S. Angelo, Naples, Italy
Dip. Biologia Strutturale e Funzionale, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Naples, Italy
References:
Amegbey, G.Y., Monzavi, H., Habibi-Nazhad, B., Bhattacharyya, S., Wishart, D.S., Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum (2003) Biochemistry, 42, pp. 8001-801
Anken, E., Braakman, I., Versatility of the endoplasmic reticulum protein folding factory (2005) Crit Rev Biochem Mol Biol, 40, pp. 191-228
Arcari, P., Fasullo, L., Masullo, M., Catanzano, F., Bocchini, V.A., NAD(P)H oxidase isolated from the archaeon Sulfolobus solfataricus is not homologous with another NADH oxidase present in the same microorganism biochemical characterization of the enzyme and cloning of the encoding gene (2000) J Biol Chem, 275, pp. 895-900
Arscott, L.D., Gromer, S., Schirmer, R.H., Becker, K., Williams Jr., C.H., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli (1997) Proc Natl Acad Sci U S A, 94, pp. 3621-3626
Bartolucci, S., Guagliardi, A., Pedone, E., De Pascale, D., Cannio, R., Camardella, L., Rossi, M., Nicolini, C., Thioredoxin from Bacillus acidocaldarius: Characterization, high-level expression in Escherichia coli and molecular modelling (1997) Biochem J, 328, pp. 277-285
Bartolucci, S., De Pascale, D., Rossi, M., Protein disulfide oxidoreductase from Pyrococcus furiosus: Biochemical properties (2001) Methods Enzymol, 334, pp. 62-73
Beeby, M., O'Connor, B.D., Ryttersgaard, C., Boutz, D.R., Perry, L.J., Yeates, T.O., The genomics of disulfide bonding and protein stabilization in thermophiles (2005) PLoS Biol, 3, pp. 1549-1558
Bhattacharyya, S., Habibi-Nazhad, B., Amegbey, G., Slupsky, C.M., Yee, A., Arrowsmith, C., Wishart, D.S., Identification of a novel archaebacterial thioredoxin: Determination of function through structure (2002) Biochemistry, 41, pp. 4760-4770
Bjornstedt, M., Hamberg, M., Kumar, S., Xue, J., Holmgren, A., Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols (1995) J Biol Chem, 270, pp. 11761-11764
Bjornstedt, M., Kumar, S., Bjorkhem, L., Spyrou, G., Holmgren, A., Selenium and the thioredoxin and glutaredoxin systems (1997) Biomed Environ Sci, 10, pp. 271-279
Buettner, C., Harney, J.W., Berry, M.J., The Caenorhabditis elegans homologue of thioredoxin reductase contains a selenocysteine insertion sequence (SECIS) element that differs from mammalian SECIS elements but directs selenocysteine incorporation (1999) J Biol Chem, 274, pp. 21598-21602
Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M.R., Bulleid, N.J., Sitia, R., ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum (2000) J Biol Chem, 275, pp. 4827-4833
Cannio, R., Fiorentino, G., Carpinelli, P., Rossi, M., Bartolucci, S., Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species (1996) J Bacteriol, 178, pp. 301-305
Chae, H.Z., Chung, S.J., Rhee, S.G., Thioredoxin dependent peroxide reductase from yeast (1994) J Biol Chem, 269, pp. 27670-27678
D'Ambrosio, K., De Simone, G., Pedone, E., Rossi, M., Bartolucci, S., Pedone, C., Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus (2004) Acta Cryst, D60, pp. 2076-2077
D'Ambrosio, K., Pedone, E., Langella, E., De Simone, G., Rossi, M., Pedone, C., Bartolucci, S., A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (2006) J Mol Biol, 362, pp. 743-752
Darby, N.J., Kemmink, J., Creighton, T.E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Dijkstra, K., Karvonen, P., Pirneskoski, A., Koivunen, P., Kivirikko, K.I., Darby, N.J., van Straaten, M., Kemmink, J., Assignment of 1H, 13C and 15N resonances of the a′ domain of protein disulfide isomerase (1999) J Biomol NMR, 14, pp. 195-196
Dixon, D.P., Van Lith, M., Edwards, R., Benham, A., Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins (2003) Antioxid Redox Signal, 5, pp. 389-396
Fabianek, R.A., Hennecke, H., Thony-Meyer, L., Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli (2000) FEMS Microbiol Rev, 24, pp. 303-316
Ferrari, D.M., Söling, H.D., The protein disulphide-isomerase family: Unraveling a string of folds (1999) Biochem J, 339, pp. 1-10
Freedman, R.B., Novel disulfide oxidoreductase in search of a function (1998) Nat Struct Biol, 5, pp. 531-532
Freedman, R.B., Klappa, P., Ruddock, L.W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Rep, 3, pp. 136-140
Fuchs, J.A., (1989) Glutathione: Chemical, biochemical, and medical aspects, p. 551. , Edited by Dolphin D, Poulsen R, and Avramovic O. New York: John Wiley and Sons, Part B, p
Ghaemmaghami, S., Huh, W.K., Bower, K., Howson, R.W., Belle, A., Dephoure, N., O'Shea, E.K., Weissman, J.S., Global analysis of protein expression in yeast (2003) Nature, 425, pp. 737-741
Ghisla, S., Massey, V., Mechanisms of flavoprotein catalyzed reactions (1989) Eur J Biochem, 181, pp. 1-17
Gladyshev, V.N., Jeang, K.T., Stadtman, T.C., Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene (1996) Proc Natl Acad Sci U S A, 93, pp. 6146-6151
Gleason, F.K., Holmgren, A., Thioredoxin and related proteins in procaryotes (1988) FEMS Microbiol Rev, 4, pp. 271-297
Grauschopf, U., Winther, J.R., Korber, P., Zander, T., Dallinger, P., Bardwell, J.C., Why is DsbA such an oxidizing disulfide catalyst? (1995) Cell, 83, pp. 947-955
Grauschopf, U., Fritz, A., Glockshuber, R., Mechanism of the electron transfer catalyst DsbB from Escherichia coli (2003) EMBO J, 22, pp. 3503-3513
Gromer, S., Merkle, H., Schirmer, R.H., Becker, K., Human placenta thioredoxin reductase: Preparation and inhibitor studies (2002) Methods Enzymol, 347, pp. 382-394
Gross, E., Sevier, C.S., Vala, A., Kaiser, C.A., Fass, D., A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p (2002) Nat Struct Biol, 9, pp. 61-67
Gross, E., Kastner, D.B., Kaiser, C.A., Fass, D., Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell (2004) Cell, 117, pp. 601-610
Guagliardi, A., De Pascale, D., Cannio, R., Nobile, V., Bartolucci, S., Rossi, M., The purification, cloning, and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (1995) J Biol Chem, 270, pp. 5748-5755
Guthapfel, R., Gueguen, P., Quemeneur, E., ATP binding and hydrolysis by the multifunctional protein disulfide isomerase (1996) J Biol Chem, 271, pp. 2663-2666
Holmgren, A., Bjornstedt, M., Thioredoxin and thioredoxin reductase (1995) Methods Enzymol, 252, pp. 199-208
Holmgren, A., Johansson, C., Berndt, C., Lonn, M.E., Hudemann, C., Lillig, C.H., Thiol redox control via thioredoxin and glutaredoxin systems (2005) Biochem Soc Trans, 33, pp. 1375-1377
Jeon, S.J., Ishikawa, K., Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1 (2002) Eur J Biochem, 269, pp. 5423-5430
Kadokura, H., Katzen, F., Beckwith, J., Protein disulfide bond formation in prokaryotes (2003) Annu Rev Biochem, 72, pp. 111-135
Kashima, Y., Ishikawa, K., Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from Pyrococcus horikoshii (2003) J Biochem (Tokyo), 134, pp. 25-29
Kawakami, R., Sakuraba, H., Kamohara, S., Goda, S., Kawarabayasi, Y., Ohshima, T., Oxidative stress response in an anaerobic hyperthermophilic archaeon: Presence of a functional peroxiredoxin in Pyrococcus horikoshii (2004) J Biochem (Tokyo), 136, pp. 541-547
Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., Creighton, T.E., Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy (1996) Biochemistry, 35, pp. 7684-7691
Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R.M., Penka, E., Nilges, M., Darby, N.J., The structure in solution of the b domain of protein disulfide isomerase (1999) J Biomol NMR, 13, pp. 357-368
Kortemme, T., Darby, N.J., Creighton, T.E., Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 14503-14511
Lappi, A., Lensink, M., Alanen, H., Salo, K., Lobell, M., Juffer, A., Ruddock, L., A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases (2004) J Mol Biol, 335, pp. 283-295
Lee, D.Y., Ahn, B.Y., Kim, K.S., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Lemaire, S.D., Miginiac-Maslow, M., The thioredoxin superfamily in Chlamydomonas reinhardtii (2004) Photosynth Res, 82, pp. 203-220
Li, K., Pasternak, C., Klug, G., Expression of the trxA gene for thioredoxin 1 in Rhodobacter sphaeroides during oxidative stress (2003) Arch Microbiol, 180, pp. 484-489
Limauro, D., Pedone, E., Pirone, L., Bartolucci, S., Identification and characterization of 1-Cys peroxiredoxin from Sulfolobus solfataricus and its involvement in the response to oxidative stress (2006) FEBS J, 273, pp. 721-731
Mallick, P., Boutz, D.R., Eisenberg, D., Yeates, T.O., Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds (2002) Proc Natl Acad Sci U S A, 99, pp. 9679-9684
Martin, J.L., Bardwell, J.C., Kuriyan, J., Crystal structure of the DsbA protein required for disulphide bond formation in vivo (1993) Nature, 365, pp. 464-468
Martin, J.L., Thioredoxin: A fold for all reasons (1995) Structure, 3, pp. 245-250
McFarlan, S.C., Terrell, C.A., Hogenkamp, H.P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J Biol Chem, 267, pp. 10561-10569
Meister, A., Glutathione metabolism and its selective modification (1988) J Biol Chem, 263, pp. 17205-17208
Messens, J., Collet, J.F., Pathways of disulfide bond formation in Escherichia coli (2006) Int J Biochem Cell Biol, 38, pp. 1050-1062
Miranda-Vizuete, A., Damdimopoulos, A.E., Gustafsson, J., Spyrou, G., Cloning, expression, and characterization of a novel Escherichia coli thioredoxin (1997) J Biol Chem, 272, pp. 30841-30847
Mittard, V., Blackledge, M.J., Stein, M., Jacquot, J.P., Marion, D., Lancelin, J.M., NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii (1997) Eur J Biochem, 243, pp. 374-383
Mizohata, E., Sakai, H., Fusatomi, E., Terada, T., Murayama, K., Shirouzu, M., Yokoyama, S., Crystal structure of an archaeal peroxiredoxin from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix K1 (2005) J Mol Biol, 354, pp. 317-329
Moore EC, Reichard P, and Thelander L. Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B. J Biol Chem 239: 3445-3452, 1964Moutevelis, E., Warwickwe, J., Prediction of pKa and redox properties in the thioredoxin superfamily (2004) Protein Sci, 13, pp. 2744-2752
Nicastro, G., de Chiara, C., Pedone, E., Tato', M., Rossi, M., Bartolucci, S., NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius: Possible determinants of protein stability (2000) Eur J Biochem, 267, pp. 403-413
Pedone, E., Bartolucci, S., Rossi, M., Saviano, M., Computational analysis of the thermal stability in thioredoxins: A molecular dynamics approach (1998) J Biomol Struct Dynamics, 16, pp. 437-446
Pedone, E., Cannio, R., Saviano, M., Rossi, M., Bartolucci, S., Prediction and experimental testing of Bacillus acidocaldarius thioredoxin stability (1999) Biochem J, 339, pp. 309-317
Pedone, E., Ren, B., Ladenstein, R., Rossi, M., Bartolucci, S., Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus (2004) Eur J Biochem, 271, pp. 3437-3448
Pedone, E., D'Ambrosio, K., De Simone, G., Rossi, M., Pedone, C., Bartolucci, S., Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (2006) J Mol Biol, 356, pp. 155-164
Pedone, E., Limauro, D., D'Alterio, R., Rossi, M., Bartolucci, S., Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (2006) FEBS J, 273, pp. 5407-5420
Prieto-Alamo, M.J., Jurado, J., Gallardo-Madueno, R., Monje-Casas, F., Holmgren, A., Pueyo, C., Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress (2000) J Biol Chem, 275, pp. 13398-13405
Prinz, W.A., Aslund, F., Holmgren, A., Beckwith, J., The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm (1997) J Biol Chem, 272, pp. 15661-15667
Prongay, A.J., Engelke, D.R., Williams Jr., C.H., Characterization of two active site mutations of thioredoxin reductase from Escherichia coli (1989) J Biol Chem, 264, pp. 2656-2664
Quemeneur, E., Guthapfel, R., Gueguen, P., A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase (1994) J Biol Chem, 269, pp. 5485-5488
Raczko, A.M., Bujnicki, J.M., Pawlowski, M., Godlewska, R., Lewandowska, M., Jagusztyn-Krynicka, E.K., Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria (2005) Microbiology, 151, pp. 219-223
Rehse, P.H., Kumei, M., Tahirov, T.H., Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus (2005) Proteins, 61, pp. 1032-1037
Ren, B., Tibbelin, G., De Pascale, D., Rossi, M., Bartolucci, S., Ladenstein, R., Crystallization and preliminary X-ray structure analysis of a hyperthermostable thioltransferase from the archaeon Pyrococcus furiosus (1997) J Struct Biol, 119, pp. 1-5
Reynolds, C.M., Meyer, J., Poole, L.B., An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum (2002) Biochemistry, 41, pp. 1990-2001
Rietsch, A., Belin, D., Martin, N., Beckwith, J., An in vivo pathway for disulfide bond isomerization in Escherichia coli (1996) Proc Natl Acad Sci U S A, 93, pp. 13048-13053
Rigobello, M.P., Scutari, G., Folda, A., Bindoli, A., Mitochondrial thioredoxin reductase inhibition by gold(I) compounds and concurrent stimulation of permeability transition and release of cytochrome c (2004) Biochem Pharmacol, 67, pp. 689-696
Rossmann, R., Stern, D., Loferer, H., Jacobi, A., Glockshuber, R., Hennecke, H., Replacement of Pro109 by His in TlpA, a thioredoxin-like protein from Bradyrhizobium japonicum, alters its redox properties but not its in vivo functions (1997) FEBS Lett, 406, pp. 249-254
Rouhier, N., Gelhaye, E., Sautiere, P.E., Brun, A., Laurent, P., Tagu, D., Gerard, J., Jacquot, J.P., Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor (2001) Plant Physiol, 127, pp. 1299-1309
Ruddock, L.W., Hirst, T.R., Feedman, R.B., pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1995) Biochem J, 315, pp. 1000-1005
Ruocco, M.R., Ruggiero, A., Masullo, L., Arcari, P., Masullo, M.A., 35 kDa NAD(P)H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase (2004) Biochimie, 86, pp. 883-892
Saarinen, M., Gleason, F.K., Eklund, H., Crystal structure of thioredoxin-2 from Anabaena (1995) Structure, 3, pp. 1097-1108
Sevier, C.S., Cuozzo, J.W., Vala, A., Aslund, F., Kaiser, C.A., A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation (2001) Nat Cell Biol, 3, pp. 874-882
Sevier, C.S., Kaiser, C.A., Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 (2006) Mol Biol Cell, 17, pp. 2256-2266
She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez M J, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A., Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, and Van der Oost J. The complete genome of the crenarchaeon Sulfolobus solfataricus P2. Proc Natl Acad Sci U S A 8: 7835-7840, 2001Silva, G., LeGall, J., Xavier, A.V., Teixeira, M., Rodrigues-Pousada, C., Molecular characterization of Desulfovibrio gigas neelaredoxin, a protein involved in oxygen detoxification in anaerobes (2001) J Bacteriol, 183, pp. 4413-4420
Sitia, R., Braakman, I., Quality control in the endoplasmic reticulum protein factory (2003) Nature, 426, pp. 891-894
Song, J., Quan, H., Wang, C., Dependence of anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochem J, 328, pp. 841-846
Tamura, T., Stadtman, T.C., A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity (1996) Proc Natl Acad Sci U S A, 3, pp. 1006-1011
Tian, G., Xiang, S., Noiva, R., Lennarz, W.J., Schindelin, H., The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites (2006) Cell, 124, pp. 61-73
Vala, A., Sevier, C.S., Kaiser, C.A., Structural determinants of substrate access to the disulfide oxidase Erv2p (2005) J Mol Biol, 354, pp. 952-966
Wang, P.F., Arscott, L.D., Gilberger, T.W., Muller, S., Williams Jr., C.H., Thioredoxin reductase from Plasmodium falciparum: Evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol (1999) Biochemistry, 38, pp. 3187-3196
Wilkinson, B., Gilbert, H.F., Protein disulfide isomerase (2004) Biochim Biophys Acta, 1699, pp. 35-44
Wood, Z.A., Schroder, E., Robin Harris, J., Poole, L.B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Wunderlich, M., Glockshuber, R., Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli (1993) Protein Sci, 2, pp. 717-726
Zillig, W., Palm, P., Reiter, W.D., Gropp, F., Puhler, G., Klenk, H.P., Comparative evaluation of gene expression in archaebacteria (1988) Eur J Biochem, 173, pp. 473-482
Carvalho, A.P., Fernandes, P.A., Ramos, M.J., Similarities and differences in the thioredoxin superfamily (2006) Prog Bio-phys Mol Biol, 91, pp. 229-248
D'Ambrosio, K., Limauro, D., Pedone, E., Galdi, I., Pedone, C., Bartolucci, S., De Simone, G., Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus (2009) Proteins, 76, pp. 995-1006
Digilio, F.A., Morra, R., Pedone, E., Bartolucci, S., Rossi, M., High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (2003) Protein Expr Purif, 30, pp. 179-184
Gruber, C.W., Cemazar, M., Heras, B., Martin, J.L., Craik, D.J., Protein disulfide isomerase: The structure of oxidative folding (2006) Trends Biochem Sci, 31, pp. 455-464
Guagliardi, A., Cerchia, L., De Rosa, M., Rossi, M., Barto-Lucci, S., Isolation of a thermostable enzyme catalyzing dis-ulfide bond formation from the archaebacterium Sulfolobus solfataricus (1992) FEBS Lett, 303, pp. 27-30
Guagliardi, A., Nobile, V., Bartolucci, S., Rossi, M., Isolation of a thioredoxin from the extreme thermophilic archae-bacterium Sulfolobus solfataricus (1994) Int J Biochem, 26, pp. 375-380
Jeon, S.-J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) Journal of Biological Chemistry, 278 (26), pp. 24174-24180. , DOI 10.1074/jbc.M300618200
Ladenstein, R., Ren, B., Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles (2006) FEBS J, 273, pp. 4170-4185
Leone, M., Di Lello, P., Ohlenschlager, O., Pedone, E.M., Bartolucci, S., Rossi, M., Di Blasio, B., Fattorusso, R., Solution structure and back-bone dynamics of the K18G=R82E Alicyclobacillus acid-ocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (2004) Biochemistry, 43, pp. 6043-6058
Limauro, D., Fiorentino, G., Bartolucci, S., How Sulfolobus responds to enviromental stress Biochemistry and Molecular Biology in the Thermophilic Archaeon S. Solfataricus, , Edited by Farina B and Faraone Mennella MR. Chapter 6: 105-130 2004. Research Signpost T.C. 37=661 (2) Fort P.O., Trivandrum-695 023, Kerala, India
Limauro, D., Saviano, M., Galdi, I., Rossi, M., Bartolucci, S., Pedone, E., Sulfolobus solfataricus protein disulphide oxido-reductase: Insight into the roles of its redox sites (2009) Protein Eng des Sel, 22, pp. 19-26
Moore, E.C., Reichard, P., Thelander, L., Enzymatic synthesis of deoxyribonucleotides.V. Purification and properties of thioredoxin reductase from Escherichia coli B (1964) J Biol Chem, 239, pp. 3445-3452
Raia, C.A., Guagliardi, A., D'Auria, S., Bartolucci, S., De Rosa, M., Rossi, M., Characterization of redox proteins from extreme thermophilic archaebacteria: Studies on alcohol dehydrogenase and thioredoxins (1995) Biosensors Bioelectron, 10, pp. 135-140
Ritz, D., Pate, H., Doan, B., Zheng, M., Aslund, F., Storz, G., Beckwith, J., Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli (2000) J Biol Chem, 275, pp. 2505-2512
She, Q., Singh, R.K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M.J., Chan-Weiher, C.C.-Y., Van Der Oostg, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (14), pp. 7835-7840. , DOI 10.1073/pnas.141222098
Song, J.-L., Quan, H., Wang, C.-C., Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochemical Journal, 328 (3), pp. 841-846
Amegbey, G. Y., Monzavi, H., Habibi-Nazhad, B., Bhattacharyya, S., Wishart, D. S., Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum (2003) Biochemistry, 42, pp. 8001-801
Arscott, L. D., Gromer, S., Schirmer, R. H., Becker, K., Williams Jr., C. H., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli (1997) Proc Natl Acad Sci U S A, 94, pp. 3621-3626
Chae, H. Z., Chung, S. J., Rhee, S. G., Thioredoxin dependent peroxide reductase from yeast (1994) J Biol Chem, 269, pp. 27670-27678
Darby, N. J., Kemmink, J., Creighton, T. E., Identifying and characterizing a structural domain of protein disulfide isomerase (1996) Biochemistry, 35, pp. 10517-11052
Dixon, D. P., Van Lith, M., Edwards, R., Benham, A., Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins (2003) Antioxid Redox Signal, 5, pp. 389-396
Fabianek, R. A., Hennecke, H., Thony-Meyer, L., Periplasmic protein thiol: disulfide oxidoreductases of Escherichia coli (2000) FEMS Microbiol Rev, 24, pp. 303-316
Ferrari, D. M., S ling, H. D., The protein disulphide-isomerase family: Unraveling a string of folds (1999) Biochem J, 339, pp. 1-10
Freedman, R. B., Novel disulfide oxidoreductase in search of a function (1998) Nat Struct Biol, 5, pp. 531-532
Freedman, R. B., Klappa, P., Ruddock, L. W., Protein disulfide isomerases exploit synergy between catalytic and specific binding domains (2002) EMBO Rep, 3, pp. 136-140
Fuchs, J. A., (1989) Glutathione: Chemical, biochemical, and medical aspects, p. 551. , Edited by Dolphin D, Poulsen R, and Avramovic O. New York: John Wiley and Sons, Part B, p
Gladyshev, V. N., Jeang, K. T., Stadtman, T. C., Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene (1996) Proc Natl Acad Sci U S A, 93, pp. 6146-6151
Gleason, F. K., Holmgren, A., Thioredoxin and related proteins in procaryotes (1988) FEMS Microbiol Rev, 4, pp. 271-297
Jeon, S. J., Ishikawa, K., Identification and characterization of thioredoxin and thioredoxin reductase from Aeropyrum pernix K1 (2002) Eur J Biochem, 269, pp. 5423-5430
Lee, D. Y., Ahn, B. Y., Kim, K. S., A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities (2000) Biochemistry, 39, pp. 6652-6659
Lemaire, S. D., Miginiac-Maslow, M., The thioredoxin superfamily in Chlamydomonas reinhardtii (2004) Photosynth Res, 82, pp. 203-220
Martin, J. L., Bardwell, J. C., Kuriyan, J., Crystal structure of the DsbA protein required for disulphide bond formation in vivo (1993) Nature, 365, pp. 464-468
Martin, J. L., Thioredoxin: A fold for all reasons (1995) Structure, 3, pp. 245-250
McFarlan, S. C., Terrell, C. A., Hogenkamp, H. P., The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium (1992) J Biol Chem, 267, pp. 10561-10569
Prieto-Alamo, M. J., Jurado, J., Gallardo-Madueno, R., Monje-Casas, F., Holmgren, A., Pueyo, C., Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress (2000) J Biol Chem, 275, pp. 13398-13405
Prinz, W. A., Aslund, F., Holmgren, A., Beckwith, J., The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm (1997) J Biol Chem, 272, pp. 15661-15667
Prongay, A. J., Engelke, D. R., Williams Jr., C. H., Characterization of two active site mutations of thioredoxin reductase from Escherichia coli (1989) J Biol Chem, 264, pp. 2656-2664
Raczko, A. M., Bujnicki, J. M., Pawlowski, M., Godlewska, R., Lewandowska, M., Jagusztyn-Krynicka, E. K., Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria (2005) Microbiology, 151, pp. 219-223
Rehse, P. H., Kumei, M., Tahirov, T. H., Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus (2005) Proteins, 61, pp. 1032-1037
Reynolds, C. M., Meyer, J., Poole, L. B., An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum (2002) Biochemistry, 41, pp. 1990-2001
Rigobello, M. P., Scutari, G., Folda, A., Bindoli, A., Mitochondrial thioredoxin reductase inhibition by gold (I) compounds and concurrent stimulation of permeability transition and release of cytochrome c (2004) Biochem Pharmacol, 67, pp. 689-696
Ruddock, L. W., Hirst, T. R., Feedman, R. B., pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol: disulphide oxidoreductase) and protein disulphide-isomerase: Studies with a novel simple peptide substrate (1995) Biochem J, 315, pp. 1000-1005
Ruocco, M. R., Ruggiero, A., Masullo, L., Arcari, P., Masullo, M. A., 35 kDa NAD (P) H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase (2004) Biochimie, 86, pp. 883-892
Sevier, C. S., Cuozzo, J. W., Vala, A., Aslund, F., Kaiser, C. A., A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation (2001) Nat Cell Biol, 3, pp. 874-882
Sevier, C. S., Kaiser, C. A., Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1 (2006) Mol Biol Cell, 17, pp. 2256-2266
Wang, P. F., Arscott, L. D., Gilberger, T. W., Muller, S., Williams Jr., C. H., Thioredoxin reductase from Plasmodium falciparum: Evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol (1999) Biochemistry, 38, pp. 3187-3196
Wood, Z. A., Schroder, E., Robin Harris, J., Poole, L. B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Carvalho, A. P., Fernandes, P. A., Ramos, M. J., Similarities and differences in the thioredoxin superfamily (2006) Prog Bio-phys Mol Biol, 91, pp. 229-248
Digilio, F. A., Morra, R., Pedone, E., Bartolucci, S., Rossi, M., High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (2003) Protein Expr Purif, 30, pp. 179-184
Gruber, C. W., Cemazar, M., Heras, B., Martin, J. L., Craik, D. J., Protein disulfide isomerase: The structure of oxidative folding (2006) Trends Biochem Sci, 31, pp. 455-464
Jeon, S. -J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) Journal of Biological Chemistry, 278 (26), pp. 24174-24180. , DOI 10. 1074/jbc. M300618200
Moore, E. C., Reichard, P., Thelander, L., Enzymatic synthesis of deoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B (1964) J Biol Chem, 239, pp. 3445-3452
Raia, C. A., Guagliardi, A., D'Auria, S., Bartolucci, S., De Rosa, M., Rossi, M., Characterization of redox proteins from extreme thermophilic archaebacteria: Studies on alcohol dehydrogenase and thioredoxins (1995) Biosensors Bioelectron, 10, pp. 135-140
She, Q., Singh, R. K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M. J., Chan-Weiher, C. C. -Y., Van Der Oostg, J., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proceedings of the National Academy of Sciences of the United States of America, 98 (14), pp. 7835-7840. , DOI 10. 1073/pnas. 141222098
Song, J. -L., Quan, H., Wang, C. -C., Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity (1997) Biochemical Journal, 328 (3), pp. 841-846
The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008)
Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts. © 2008 Mary Ann Liebert, Inc.
Disulfide bonds are required for the stability and function of many proteins. A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans. The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm. Recently the results from genome analysis suggested an important role for disulfide bonds in the structural stabilization of intracellular proteins from thermophiles. A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles. Here we focus on the structural and functional characterization of PDO correlated with the multifunctional eukaryotic PDI. In addition, we highlight the chimeric nature of the machinery for oxidative protein folding in thermophiles in comparison with the mesophilic bacterial and eukaryal counterparts. © 2008 Mary Ann Liebert, Inc.
The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008)
| ▼ Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions |
The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008)
Other filter: ([btitle,keywords] "Glutaredoxin" OR [bt ...
Ruggiero A, Smaldone G, Esposito L, Balasco N, Vitagliano L
* Loop size optimization induces a strong thermal stabilization of the thioredoxin fold (193 views)
Febs J (ISSN: 1742-464xlinking), 2019 May; 286(9): 1752-1764.
Impact Factor: 3.129
View Export to BibTeX Export to EndNote
Calce E, Vitale RM, Scaloni A, Amodeo P, De Luca S
* Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides (597 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2015; 47(8): 1507-1515.
Impact Factor: 3.196
View Export to BibTeX Export to EndNote
Ringhieri P, Diaferia C, Galdiero S, Palumbo R, Morelli G, Accardo A
* Liposomal doxorubicin doubly functionalized with CCK8 and R8 peptide sequences for selective intracellular drug delivery (451 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015; 21(5): 415-425.
Impact Factor: 1.951
View Export to BibTeX Export to EndNote
Benetti F, Biarnés X, Attanasio F, Giachin G, Rizzarelli E, Legname G
* Structural determinants in prion protein folding and stability (596 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 0022-2836linking), 2014 Nov 11; 426(22): 3796-3810.
Impact Factor: 4.333
View Export to BibTeX Export to EndNote
Limauro D, De Simone G, Pirone L, Bartolucci S, D'Ambrosio K, Pedone E
* Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase (429 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2014 Mar; 18(2): 219-228.
Impact Factor: 2.306
View Export to BibTeX Export to EndNote
Messori L, Scaletti F, Massai L, Cinellu MA, Russo Krauss I, Di Martino G, Vergara A, Paduano L, Merlino A
* Interactions of gold-based drugs with proteins: crystal structure of the adduct formed between ribonuclease A and a cytotoxic gold(III) compound (339 views)
Metallomics (ISSN: 1756-5901, 1756-591x), 2014; 6(2): 233-236.
Impact Factor: 3.585
View Export to BibTeX Export to EndNote
Petruk AA, Varriale S, Coscia MR, Mazzarella L, Merlino A, Oreste U
* The Structure Of The Cd3 Zeta Zeta Transmembrane Dimer In Popc And Raft-Like Lipid Bilayer: A Molecular Dynamics Study (442 views)
Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002e, 0005-2736print), 2013 Nov; 1828(11): 2637-2645.
Impact Factor: 3.498
View Export to BibTeX Export to EndNote
Del Giudice I, Limauro D, Pedone E, Bartolucci S, Fiorentino G
* A novel arsenate reductase from the bacterium Thermus thermophilus HB27: Its role in arsenic detoxification (420 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Oct; 1834(10): 2071-2079.
Impact Factor: 3.191
View Export to BibTeX Export to EndNote
Cammisa M, Correra A, Andreotti G, Cubellis MV
* Fabry_CEP: a tool to identify Fabry mutations responsive to pharmacological chaperones (415 views)
Orphanet Journal Of Rare Diseases (ISSN: 1750-1172), 2013 Jul 24; 8: 111-111.
Impact Factor: 3.958
View Export to BibTeX Export to EndNote
Balasco N, Esposito L, De Simone A, Vitagliano L
* Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms (353 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2013 Jul; 22(7): 1016-1023.
Impact Factor: 2.861
View Export to BibTeX Export to EndNote
Avitabile C, Capparelli R, Rigano MM, Fulgione A, Barone A, Pedone C, Romanelli A
* Antimicrobial peptides from plants: Stabilization of the γ core of a tomato defensin by intramolecular disulfide bond (755 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 240-245.
Impact Factor: 1.862
View Export to BibTeX Export to EndNote
Bera S, De Rosa V, Rachidi W, Diamond AM
* Does a role for selenium in DNA damage repair explain apparent controversies in its use in chemoprevention? (639 views)
Mutagenesismutagenesis (ISSN: 0267-8357, 1464-3804electronic, 0267-8357linking), 2013 Mar; 28(2): 127-134.
Impact Factor: 3.497
View Export to BibTeX Export to EndNote
Balasco N, Esposito L, De Simone A, Vitagliano L
* FOR the RECORD: Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms (539 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2013; 22(7): 1016-1023.
Impact Factor: 2.861
View Export to BibTeX Export to EndNote
Russo Krauss I, Sica F, Mattia CA, Merlino A
* Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data (461 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
Impact Factor: 2.464
View Export to BibTeX Export to EndNote
Esposito L, Ruggiero A, Masullo M, Ruocco MR, Lamberti A, Arcari P, Zagari A, Vitagliano L
* Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability (300 views)
J Struct Biol (ISSN: 1047-8477, 1047-8477linking), 2012 Feb; 177(2): 506-512.
Impact Factor: 3.361
View Export to BibTeX Export to EndNote
De Rosa V, Erkekoǧlu P, Forestier A, Favier A, Hincal F, Diamond AM, Douki T, Rachidi W
* Low doses of selenium specifically stimulate the repair of oxidative DNA damage in LNCaP prostate cancer cells (550 views)
Free Radic Res Free Radical Research (ISSN: 1071-5762), 2012; 46(2): 105-115.
Impact Factor: 3.279
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Cuzzocrea S, Iavicoli I, Rizzarelli E, Calabrese EJ
* Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity (881 views)
Molecular Aspects Of Medicine (ISSN: 1872-9452, 0098-2997), 2011 Sep; 32(4-6): 279-304.
Impact Factor: 9.97
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S
* Multiple catalytically active thioredoxin folds: a winning strategy for many functions (725 views)
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
Impact Factor: 7.047
View Export to BibTeX Export to EndNote
Limauro D, D'Ambrosio K, Langella E, De Simone G, Galdi I, Pedone C, Pedone E, Bartolucci S
* Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus (373 views)
Biochimie (ISSN: 1638-6183, 0300-9084, 1638-6183electronic), 2010 Oct; 92(10): 1435-1444.
Impact Factor: 3.787
View Export to BibTeX Export to EndNote
De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (398 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
View Export to BibTeX Export to EndNote
Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (316 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
View Export to BibTeX Export to EndNote
Bellia F, Calabrese V, Guarino F, Cavallaro M, Cornelius C, De Pinto V, Rizzarelli E
* Carnosinase levels in aging brain: redox state induction and cellular stress response (445 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2759-2775.
Impact Factor: 7.581
View Export to BibTeX Export to EndNote
Alterio V, Hilvo M, Di Fiore A, Supuran CT, Pan P, Parkkila S, Scaloni A, Pastorek J, Pastorekova S, Pedone C, Scozzafava A, Monti SM, De Simone G
* Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX (571 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2009 Sep 22; 106(38): 16233-16238.
Impact Factor: 9.432
View Export to BibTeX Export to EndNote
D'Ambrosio K, Limauro D, Pedone E, Galdi I, Pedone C, Bartolucci S, De Simone G
* Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus (469 views)
Proteins (ISSN: 1097-0134, 0887-3585, 1097-0134electronic), 2009 Sep; 76(4): 995-1006.
Impact Factor: 3.085
View Export to BibTeX Export to EndNote
Ruggiero A, Lanzotti MA, Ruocco MR, Grimaldi P, Marasco D, Arcari P, Masullo M, Zagari A, Vitagliano L
* Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus (337 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2009 Jun; 65: 604-607.
Impact Factor: 0.551
View Export to BibTeX Export to EndNote
Accardo A, Tesauro D, Morisco A, Mangiapia G, Vaccaro M, Gianolio E, Heenan RK, Paduano L, Morelli G
* Micelles obtained by aggregation of gemini surfactants containing the CCK8 peptide and a gadolinium complex (398 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257linking), 2009 May; 14(4): 587-599.
Impact Factor: 3.415
View Export to BibTeX Export to EndNote
Ruggiero A, Masullo M, Ruocco MR, Grimaldi P, Lanzotti MA, Arcari P, Zagari A, Vitagliano L
* Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions (347 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2009 Mar; 1794(3): 554-562.
Impact Factor: 2.48
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Mancuso C, Barone E, Calafato S, Bates T, Rizzarelli E, Kostova AT
* Vitagenes, dietary antioxidants and neuroprotection in neurodegenerative diseases (1145 views)
Frontiers In Bioscience (ISSN: 1093-4715, 1093-9946), 2009 Jan 1; 14: 376-397.
Impact Factor: 3.736
View Export to BibTeX Export to EndNote
Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (234 views)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Mancuso C, Pennisi G, Calafato S, Bellia F, Bates TE, Giuffrida Stella AM, Schapira T, Dinkova Kostova AT, Rizzarelli E
* Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity (1232 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2008 Dec; 33(12): 2444-2471.
Impact Factor: 2.26
View Export to BibTeX Export to EndNote
Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (459 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
View Export to BibTeX Export to EndNote
Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (578 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
View Export to BibTeX Export to EndNote
Grimaldi P, Ruocco MR, Lanzotti MA, Ruggiero A, Ruggiero I, Arcari P, Vitagliano L, Masullo M
* Characterisation of the components of the thioredoxin system in the archaeon Sulfolobus solfataricus (356 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2008 Jul; 12(4): 553-562.
Impact Factor: 1.782
View Export to BibTeX Export to EndNote
Limauro D, Pedone E, Galdi I, Bartolucci S
* Peroxiredoxins as cellular guardians in Sulfolobus solfataricus - characterization of Bcp1, Bcp3 and Bcp4 (366 views)
Febs Journal (ISSN: 1742-464x), 2008 May; 275(9): 2067-2077.
Impact Factor: 3.139
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (337 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (328 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
View Export to BibTeX Export to EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (485 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (475 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
View Export to BibTeX Export to EndNote
De Simone G, Vitale RM, Di Fiore A, Pedone C, Scozzafava A, Montero JL, Winum JY, Supuran CT
* Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Sep 7; 49(18): 5544-5551.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (391 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
View Export to BibTeX Export to EndNote
Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (318 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
View Export to BibTeX Export to EndNote
Ruggiero A, Ruocco MR, Grimaldi P, Arcari P, Masullo M, Zagari A, Vitagliano L
* Crystallization and preliminary X-ray crystallographic analysis of Sulfolobus solfataricus thioredoxin reductase (319 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2005 Oct; 61: 906-909.
Impact Factor: 0.568
View Export to BibTeX Export to EndNote
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (442 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (367 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Esposito L, De Simone A, Zagari A, Vitagliano L
* Correlation Between Omega And Psi Dihedral Angles In Protein Structures (592 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005 Apr 1; 347(3): 483-487.
Impact Factor: 5.229
View Export to BibTeX Export to EndNote
Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (443 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Sep 27; 279(35): 36753-36760.
Impact Factor: 6.355
View Export to BibTeX Export to EndNote
Pedone E, Bartolucci S, Fiorentino G
* Sensing and adapting to environmental stress: The Archaeal tactic (327 views)
Frontiers In Bioscience (ISSN: 1093-9946, 1093-4715), 2004 Sep 1; 9: 2909-2926.
Impact Factor: 3.226
View Export to BibTeX Export to EndNote
Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (390 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
View Export to BibTeX Export to EndNote
Leone M, Di Lello P, Ohlenschläger O, Pedone E, Bartolucci S, Rossi M, Di Blasio B, Pedone C, Saviano M, Isernia C, Fattorusso R
* Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (438 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058.
Impact Factor: 4.008
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (384 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Pedone E, Bartolucci S, Rossi M, Pierfederici FM, Scire A, Cacciamani T, Tanfani F
* Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study (537 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2003 Sep 1; 373: 875-883.
Impact Factor: 4.101
View Export to BibTeX Export to EndNote
Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (355 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
View Export to BibTeX Export to EndNote
Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (233 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
View Export to BibTeX Export to EndNote
Bartolucci S, De Simone G, Galdiero S, Improta R, Menchise V, Pedone C, Pedone E, Saviano M
* An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius (326 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4285-4289.
Impact Factor: 4.175
View Export to BibTeX Export to EndNote
D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
* Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione (304 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003 Jun; 59: 1043-1045.
Impact Factor: 2.208
View Export to BibTeX Export to EndNote
Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (424 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
View Export to BibTeX Export to EndNote
Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (387 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
View Export to BibTeX Export to EndNote
* Loop size optimization induces a strong thermal stabilization of the thioredoxin fold (193 views)
Febs J (ISSN: 1742-464xlinking), 2019 May; 286(9): 1752-1764.
Impact Factor: 3.129
View Export to BibTeX Export to EndNote
Calce E, Vitale RM, Scaloni A, Amodeo P, De Luca S
* Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides (597 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2015; 47(8): 1507-1515.
Impact Factor: 3.196
View Export to BibTeX Export to EndNote
Ringhieri P, Diaferia C, Galdiero S, Palumbo R, Morelli G, Accardo A
* Liposomal doxorubicin doubly functionalized with CCK8 and R8 peptide sequences for selective intracellular drug delivery (451 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015; 21(5): 415-425.
Impact Factor: 1.951
View Export to BibTeX Export to EndNote
Benetti F, Biarnés X, Attanasio F, Giachin G, Rizzarelli E, Legname G
* Structural determinants in prion protein folding and stability (596 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 0022-2836linking), 2014 Nov 11; 426(22): 3796-3810.
Impact Factor: 4.333
View Export to BibTeX Export to EndNote
Limauro D, De Simone G, Pirone L, Bartolucci S, D'Ambrosio K, Pedone E
* Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase (429 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2014 Mar; 18(2): 219-228.
Impact Factor: 2.306
View Export to BibTeX Export to EndNote
Messori L, Scaletti F, Massai L, Cinellu MA, Russo Krauss I, Di Martino G, Vergara A, Paduano L, Merlino A
* Interactions of gold-based drugs with proteins: crystal structure of the adduct formed between ribonuclease A and a cytotoxic gold(III) compound (339 views)
Metallomics (ISSN: 1756-5901, 1756-591x), 2014; 6(2): 233-236.
Impact Factor: 3.585
View Export to BibTeX Export to EndNote
Petruk AA, Varriale S, Coscia MR, Mazzarella L, Merlino A, Oreste U
* The Structure Of The Cd3 Zeta Zeta Transmembrane Dimer In Popc And Raft-Like Lipid Bilayer: A Molecular Dynamics Study (442 views)
Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002e, 0005-2736print), 2013 Nov; 1828(11): 2637-2645.
Impact Factor: 3.498
View Export to BibTeX Export to EndNote
Del Giudice I, Limauro D, Pedone E, Bartolucci S, Fiorentino G
* A novel arsenate reductase from the bacterium Thermus thermophilus HB27: Its role in arsenic detoxification (420 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Oct; 1834(10): 2071-2079.
Impact Factor: 3.191
View Export to BibTeX Export to EndNote
Cammisa M, Correra A, Andreotti G, Cubellis MV
* Fabry_CEP: a tool to identify Fabry mutations responsive to pharmacological chaperones (415 views)
Orphanet Journal Of Rare Diseases (ISSN: 1750-1172), 2013 Jul 24; 8: 111-111.
Impact Factor: 3.958
View Export to BibTeX Export to EndNote
Balasco N, Esposito L, De Simone A, Vitagliano L
* Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms (353 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2013 Jul; 22(7): 1016-1023.
Impact Factor: 2.861
View Export to BibTeX Export to EndNote
Avitabile C, Capparelli R, Rigano MM, Fulgione A, Barone A, Pedone C, Romanelli A
* Antimicrobial peptides from plants: Stabilization of the γ core of a tomato defensin by intramolecular disulfide bond (755 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2013 Apr; 19(4): 240-245.
Impact Factor: 1.862
View Export to BibTeX Export to EndNote
Bera S, De Rosa V, Rachidi W, Diamond AM
* Does a role for selenium in DNA damage repair explain apparent controversies in its use in chemoprevention? (639 views)
Mutagenesismutagenesis (ISSN: 0267-8357, 1464-3804electronic, 0267-8357linking), 2013 Mar; 28(2): 127-134.
Impact Factor: 3.497
View Export to BibTeX Export to EndNote
Balasco N, Esposito L, De Simone A, Vitagliano L
* FOR the RECORD: Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms (539 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2013; 22(7): 1016-1023.
Impact Factor: 2.861
View Export to BibTeX Export to EndNote
Russo Krauss I, Sica F, Mattia CA, Merlino A
* Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data (461 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
Impact Factor: 2.464
View Export to BibTeX Export to EndNote
Esposito L, Ruggiero A, Masullo M, Ruocco MR, Lamberti A, Arcari P, Zagari A, Vitagliano L
* Crystallographic and spectroscopic characterizations of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability (300 views)
J Struct Biol (ISSN: 1047-8477, 1047-8477linking), 2012 Feb; 177(2): 506-512.
Impact Factor: 3.361
View Export to BibTeX Export to EndNote
De Rosa V, Erkekoǧlu P, Forestier A, Favier A, Hincal F, Diamond AM, Douki T, Rachidi W
* Low doses of selenium specifically stimulate the repair of oxidative DNA damage in LNCaP prostate cancer cells (550 views)
Free Radic Res Free Radical Research (ISSN: 1071-5762), 2012; 46(2): 105-115.
Impact Factor: 3.279
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Cuzzocrea S, Iavicoli I, Rizzarelli E, Calabrese EJ
* Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity (881 views)
Molecular Aspects Of Medicine (ISSN: 1872-9452, 0098-2997), 2011 Sep; 32(4-6): 279-304.
Impact Factor: 9.97
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S
* Multiple catalytically active thioredoxin folds: a winning strategy for many functions (725 views)
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
Impact Factor: 7.047
View Export to BibTeX Export to EndNote
Limauro D, D'Ambrosio K, Langella E, De Simone G, Galdi I, Pedone C, Pedone E, Bartolucci S
* Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus (373 views)
Biochimie (ISSN: 1638-6183, 0300-9084, 1638-6183electronic), 2010 Oct; 92(10): 1435-1444.
Impact Factor: 3.787
View Export to BibTeX Export to EndNote
De Simone G, Supuran CT
* Carbonic anhydrase IX: Biochemical and crystallographic characterization of a novel antitumor target (398 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2010 Feb; 1804(2): 404-409.
Impact Factor: 2.773
View Export to BibTeX Export to EndNote
Ruggiero A, Masullo M, Marasco D, Ruocco MR, Grimaldi P, Arcari P, Zagari A, Vitagliano L
* The dimeric structure of Sulfolobus solfataricus thioredoxin A2 and the basis of its thermostability (316 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2009 Dec; 77(4): 1004-1008.
Impact Factor: 3.085
View Export to BibTeX Export to EndNote
Bellia F, Calabrese V, Guarino F, Cavallaro M, Cornelius C, De Pinto V, Rizzarelli E
* Carnosinase levels in aging brain: redox state induction and cellular stress response (445 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2759-2775.
Impact Factor: 7.581
View Export to BibTeX Export to EndNote
Alterio V, Hilvo M, Di Fiore A, Supuran CT, Pan P, Parkkila S, Scaloni A, Pastorek J, Pastorekova S, Pedone C, Scozzafava A, Monti SM, De Simone G
* Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX (571 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2009 Sep 22; 106(38): 16233-16238.
Impact Factor: 9.432
View Export to BibTeX Export to EndNote
D'Ambrosio K, Limauro D, Pedone E, Galdi I, Pedone C, Bartolucci S, De Simone G
* Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus (469 views)
Proteins (ISSN: 1097-0134, 0887-3585, 1097-0134electronic), 2009 Sep; 76(4): 995-1006.
Impact Factor: 3.085
View Export to BibTeX Export to EndNote
Ruggiero A, Lanzotti MA, Ruocco MR, Grimaldi P, Marasco D, Arcari P, Masullo M, Zagari A, Vitagliano L
* Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus (337 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2009 Jun; 65: 604-607.
Impact Factor: 0.551
View Export to BibTeX Export to EndNote
Accardo A, Tesauro D, Morisco A, Mangiapia G, Vaccaro M, Gianolio E, Heenan RK, Paduano L, Morelli G
* Micelles obtained by aggregation of gemini surfactants containing the CCK8 peptide and a gadolinium complex (398 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257linking), 2009 May; 14(4): 587-599.
Impact Factor: 3.415
View Export to BibTeX Export to EndNote
Ruggiero A, Masullo M, Ruocco MR, Grimaldi P, Lanzotti MA, Arcari P, Zagari A, Vitagliano L
* Structure and stability of a thioredoxin reductase from Sulfolobus solfataricus: A thermostable protein with two functions (347 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2009 Mar; 1794(3): 554-562.
Impact Factor: 2.48
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Mancuso C, Barone E, Calafato S, Bates T, Rizzarelli E, Kostova AT
* Vitagenes, dietary antioxidants and neuroprotection in neurodegenerative diseases (1145 views)
Frontiers In Bioscience (ISSN: 1093-4715, 1093-9946), 2009 Jan 1; 14: 376-397.
Impact Factor: 3.736
View Export to BibTeX Export to EndNote
Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (234 views)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
View Export to BibTeX Export to EndNote
Calabrese V, Cornelius C, Mancuso C, Pennisi G, Calafato S, Bellia F, Bates TE, Giuffrida Stella AM, Schapira T, Dinkova Kostova AT, Rizzarelli E
* Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity (1232 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2008 Dec; 33(12): 2444-2471.
Impact Factor: 2.26
View Export to BibTeX Export to EndNote
Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (459 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
View Export to BibTeX Export to EndNote
Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (578 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
View Export to BibTeX Export to EndNote
Grimaldi P, Ruocco MR, Lanzotti MA, Ruggiero A, Ruggiero I, Arcari P, Vitagliano L, Masullo M
* Characterisation of the components of the thioredoxin system in the archaeon Sulfolobus solfataricus (356 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2008 Jul; 12(4): 553-562.
Impact Factor: 1.782
View Export to BibTeX Export to EndNote
Limauro D, Pedone E, Galdi I, Bartolucci S
* Peroxiredoxins as cellular guardians in Sulfolobus solfataricus - characterization of Bcp1, Bcp3 and Bcp4 (366 views)
Febs Journal (ISSN: 1742-464x), 2008 May; 275(9): 2067-2077.
Impact Factor: 3.139
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (337 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
View Export to BibTeX Export to EndNote
Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (328 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
View Export to BibTeX Export to EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (485 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M
* Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 30; 49(24): 7054-7062.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (475 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
View Export to BibTeX Export to EndNote
De Simone G, Vitale RM, Di Fiore A, Pedone C, Scozzafava A, Montero JL, Winum JY, Supuran CT
* Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX (474 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Sep 7; 49(18): 5544-5551.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (391 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
View Export to BibTeX Export to EndNote
Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (318 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
View Export to BibTeX Export to EndNote
Ruggiero A, Ruocco MR, Grimaldi P, Arcari P, Masullo M, Zagari A, Vitagliano L
* Crystallization and preliminary X-ray crystallographic analysis of Sulfolobus solfataricus thioredoxin reductase (319 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2005 Oct; 61: 906-909.
Impact Factor: 0.568
View Export to BibTeX Export to EndNote
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (442 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (367 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Esposito L, De Simone A, Zagari A, Vitagliano L
* Correlation Between Omega And Psi Dihedral Angles In Protein Structures (592 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005 Apr 1; 347(3): 483-487.
Impact Factor: 5.229
View Export to BibTeX Export to EndNote
Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (443 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Sep 27; 279(35): 36753-36760.
Impact Factor: 6.355
View Export to BibTeX Export to EndNote
Pedone E, Bartolucci S, Fiorentino G
* Sensing and adapting to environmental stress: The Archaeal tactic (327 views)
Frontiers In Bioscience (ISSN: 1093-9946, 1093-4715), 2004 Sep 1; 9: 2909-2926.
Impact Factor: 3.226
View Export to BibTeX Export to EndNote
Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (390 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
View Export to BibTeX Export to EndNote
Leone M, Di Lello P, Ohlenschläger O, Pedone E, Bartolucci S, Rossi M, Di Blasio B, Pedone C, Saviano M, Isernia C, Fattorusso R
* Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (438 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058.
Impact Factor: 4.008
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (384 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Pedone E, Bartolucci S, Rossi M, Pierfederici FM, Scire A, Cacciamani T, Tanfani F
* Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study (537 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2003 Sep 1; 373: 875-883.
Impact Factor: 4.101
View Export to BibTeX Export to EndNote
Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (355 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
View Export to BibTeX Export to EndNote
Digilio Filomena A, Morra R, Pedone E, Bartolucci S, Rossi M
* High-level expression of Aliciclobacillus acidocaldarius thioredoxin in Pichia pastoris and Bacillus subtilis (233 views)
Protein Expr Purif (ISSN: 1046-5928), 2003 Sep; 30(2): 179-184.
Impact Factor: 1.47
View Export to BibTeX Export to EndNote
Bartolucci S, De Simone G, Galdiero S, Improta R, Menchise V, Pedone C, Pedone E, Saviano M
* An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius (326 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4285-4289.
Impact Factor: 4.175
View Export to BibTeX Export to EndNote
D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
* Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione (304 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003 Jun; 59: 1043-1045.
Impact Factor: 2.208
View Export to BibTeX Export to EndNote
Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (424 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
View Export to BibTeX Export to EndNote
Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (387 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
View Export to BibTeX Export to EndNote
58 Records (57 excluding Abstracts).
Total impact factor: 224.564 (220.606 excluding Abstracts).
Total 5 year impact factor: 226.25 (220.87 excluding Abstracts).
Total impact factor: 224.564 (220.606 excluding Abstracts).
Total 5 year impact factor: 226.25 (220.87 excluding Abstracts).
315 views. Last view on Sunday 05 February 2023, 9:50:50
ibb.cnr.it
